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Database: UniProt
Entry: I6L925_STRMU
LinkDB: I6L925_STRMU
Original site: I6L925_STRMU 
ID   I6L925_STRMU            Unreviewed;       161 AA.
AC   I6L925;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   RecName: Full=Ascorbate-specific PTS system EIIA component {ECO:0000256|ARBA:ARBA00041175};
DE   AltName: Full=Ascorbate-specific phosphotransferase enzyme IIA component {ECO:0000256|ARBA:ARBA00042072};
GN   Name=ptxA {ECO:0000313|EMBL:AAN58039.1};
GN   OrderedLocusNames=SMU_272 {ECO:0000313|EMBL:AAN58039.1};
OS   Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=210007 {ECO:0000313|EMBL:AAN58039.1, ECO:0000313|Proteomes:UP000002512};
RN   [1] {ECO:0000313|EMBL:AAN58039.1, ECO:0000313|Proteomes:UP000002512}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700610 / UA159 {ECO:0000313|Proteomes:UP000002512};
RX   PubMed=12397186; DOI=10.1073/pnas.172501299;
RA   Ajdic D., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA   Primeaux C., Tian R., Kenton S., Jia H., Lin S., Qian Y., Li S., Zhu H.,
RA   Najar F., Lai H., White J., Roe B.A., Ferretti J.J.;
RT   "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT   pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
CC   -!- FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase
CC       system (sugar PTS), a major carbohydrate active transport system,
CC       catalyzes the phosphorylation of incoming sugar substrates
CC       concomitantly with their translocation across the cell membrane. The
CC       enzyme II UlaABC PTS system is involved in ascorbate transport.
CC       {ECO:0000256|ARBA:ARBA00037387}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR   EMBL; AE014133; AAN58039.1; -; Genomic_DNA.
DR   RefSeq; NP_720733.1; NC_004350.2.
DR   RefSeq; WP_002262725.1; NC_004350.2.
DR   AlphaFoldDB; I6L925; -.
DR   SMR; I6L925; -.
DR   STRING; 210007.SMU_272; -.
DR   GeneID; 66818242; -.
DR   KEGG; smu:SMU_272; -.
DR   PATRIC; fig|210007.7.peg.237; -.
DR   eggNOG; COG1762; Bacteria.
DR   HOGENOM; CLU_072531_2_0_9; -.
DR   OrthoDB; 369398at2; -.
DR   PhylomeDB; I6L925; -.
DR   Proteomes; UP000002512; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   CDD; cd00211; PTS_IIA_fru; 1.
DR   InterPro; IPR016152; PTrfase/Anion_transptr.
DR   InterPro; IPR002178; PTS_EIIA_type-2_dom.
DR   PANTHER; PTHR36203; ASCORBATE-SPECIFIC PTS SYSTEM EIIA COMPONENT; 1.
DR   PANTHER; PTHR36203:SF1; ASCORBATE-SPECIFIC PTS SYSTEM EIIA COMPONENT; 1.
DR   Pfam; PF00359; PTS_EIIA_2; 1.
DR   SUPFAM; SSF55804; Phoshotransferase/anion transport protein; 1.
DR   PROSITE; PS51094; PTS_EIIA_TYPE_2; 1.
PE   4: Predicted;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002512}.
FT   DOMAIN          6..148
FT                   /note="PTS EIIA type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51094"
SQ   SEQUENCE   161 AA;  17679 MW;  F819C51F5F5ED295 CRC64;
     MNLAQAFKEN HSIRLGLTAK DWKEAVKLSV TPLIESGAVK PEYYNAIIES TESYGPYYIL
     MPGMAMPHAR PEAGVQRDAF SLVTLTEPVT FTDGKEVQVL LALAATSSKI HTSVAIPQII
     ALFELDHSIE RLVNCKTPEE VLAMVEESKS SPYLEGLDLD S
//
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